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Cited by 292Protein Kinase Regulation and GTPase SignalingCellular transport and secretionProtein Tyrosine Phosphatases

Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.

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Hofer, F, Fields, S, Schneider, C, Martin, G S·1994·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.91.23.11089PMC PMC45172
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Abstract

The yeast two-hybrid system was used to identify proteins that interact with Ras. The H-Ras protein was found to interact with a guanine nucleotide dissociation stimulator (GDS) that has been previously shown to regulate guanine nucleotide exchange on another member of the Ras protein family, Ral. The interaction is mediated by the C-terminal, noncatalytic segment of the RalGDS and can be detected both in vivo, using the two-hybrid system, and in vitro, with purified recombinant proteins. The interaction of the RalGDS C-terminal segment with Ras is specific, dependent on activation of Ras by GTP, and blocked by a mutation that affects Ras effector function. These characteristics are similar to those previously demonstrated for the interaction between Ras and its putative effector, Raf, suggesting that the RalGDS may also be a Ras effector. Consistent with this idea, the RalGDS was found to inhibit the binding of Raf to Ras.

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  • Ral can be activated either by Ras indirectly via a Ral-GEF or by Ca2+/calmodulin binding.

    “Ral can be activated either by Ras indirectly via a Ral-GEF (Guanine nucleotide Exchange Factor) or by Ca 2 þ /calmodulin binding (Hofer et al, 1994(Hofer et al, , 1998;;Kikuchi et al, 1994;Wolthuis et al, 1998;Wang and Roufogalis, 1999;Wolthuis and Bos, 1999;Harvey et al, 2008)”

    From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Hofer et al, 1994

  • KRAS activation leads to downstream signaling of three major pathways: MAPK, PI3K-AKT-mTOR, and TIAM1-RAC/RAL.

    “KRAS activation leads to downstream signaling of three major pathways: the MAP kinase pathway, PI3K-AKT-mTOR pathway, and the tumour invasion and metastasis-inducing protein 1 (TIAM1-RAC) and RAS-related protein (RAL) pathways (Fig. 3).”

    From Drugging KRAS: Current perspectives and state-of-art review (2022) · cites this paper as [39]

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Authors
Hofer, F., Fields, S., Schneider, C., & Martin, G. S.
Affiliations
University of California, Berkeley (US)
ORCID
Fields, S
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1994-11-08
Volume
91
Issue
23
Pages
11089-11093
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.91.23.11089
PMC
PMC45172
OpenAlex
W2012189464
Cited by
287
References
30
Citations by year
2026: 2 · 2025: 5 · 2024: 5 · 2023: 6 · 2022: 13 · 2021: 4 · 2020: 9 · 2019: 4 · 2018: 5 · 2017: 8 · 2016: 8 · 2015: 6 · 2014: 3 · 2013: 9
FWCI
9.87
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Cancer Institute (CA17542, P01CA028146, CA-28146)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords
Ras, RalGDS, protein-protein interaction, Ras effectors, guanine nucleotide exchange, Ras activation, Raf, Ras family
MeSH terms
Amino Acid Sequence, Binding Sites, Binding, Competitive, Humans, Molecular Sequence Data, Protein Binding, Proto-Oncogene Proteins, Structure-Activity Relationship, Proto-Oncogene Proteins p21(ras), Mutagenesis, Site-Directed, Sequence Alignment, Protein Serine-Threonine Kinases, Sequence Homology, Amino Acid, GTP-Binding Proteins, Proto-Oncogene Proteins c-raf, ral GTP-Binding Proteins, In Vitro Techniques

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